8thw

Cac1 PIP motif bound to PCNA

Method: X-RAY DIFFRACTION Dmax: 96.5 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Proliferating cell nuclear antigen,Chromatin assembly factor 1 subunit p90

Saccharomyces cerevisiae

UniProt P15873

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–258 Chain B; UniProt 1–258 Chain C; UniProt 1–258 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1M magnesium acetate tetrahydrate (Mg Ac4H) and 11% w/v PEG3350 Resolution 2.60 Å R-free 0.267

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

55 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PCNA_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–265; UniProt 1–258 Author chain B; PDBConstruct 8–265; UniProt 1–258 Author chain C; PDBConstruct 8–265; UniProt 1–258

Proliferating cell nuclear antigen,Chromatin assembly factor 1 subunit p90

Saccharomyces cerevisiae

UniProt Q12495

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 222–240 Chain B; UniProt 222–240 Chain C; UniProt 222–240 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1M magnesium acetate tetrahydrate (Mg Ac4H) and 11% w/v PEG3350 Resolution 2.60 Å R-free 0.267

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

3 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RLF2_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 271–289; UniProt 222–240 Author chain B; PDBConstruct 271–289; UniProt 222–240 Author chain C; PDBConstruct 271–289; UniProt 222–240

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8thw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8thw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8thw
Deposition date deposition_date2023-07-18
最后修订 last_revision2024-09-18
Structure title titleCac1 PIP motif bound to PCNA
Keywords keywords;Sliding clamp, histone chaperone, replication-coupled nucleosome assembly, chromatin assembly, gene silencing, protein complex, PIP, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier33.85
Radius of gyration Rg (electron density) rg_electron32.78
Forward intensity I(0) i0117958000.00
Molecular weight molecular_weight89836.0 kDa
Excluded volume excluded_volume113930 ų
Envelope volume envelope_volume155730 ų
Hydration-shell volume shell_volume38356 ų
Envelope diameter envelope_diameter100.1
Shell Rg shell_rg41.43
Envelope Rg envelope_rg31.46
Shape Rg shape_rg32.78
Total Rg total_rg33.56
Total atoms total_atoms6315
Residues n_residues801
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax96.5
Rg (real space) rg_real33.68
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real1.1800e+08
I(0) uncertainty (real space) i0_real_error1.9840e+06
Rg (reciprocal space) rg_reciprocal33.79
I(0) (reciprocal space) i0_reciprocal118000000.0000
Solution quality estimate total_estimate0.8954
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary49.3
Skewness Skewness skewness-0.034
Kurtosis Kurtosis kurtosis-0.810
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha46550000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.967; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.741

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)